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CD22 molecule
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| Identifiers | ||||||||||||||
| Symbols | CD22; MGC130020; SIGLEC-2; SIGLEC2 | |||||||||||||
| External IDs | OMIM: 107266 MGI: 88322 HomoloGene: 31052 | |||||||||||||
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| RNA expression pattern | ||||||||||||||
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| Orthologs | ||||||||||||||
| Human | Mouse | |||||||||||||
| Entrez | 933 | 12483 | ||||||||||||
| Ensembl | ENSG00000012124 | ENSMUSG00000030577 | ||||||||||||
| Uniprot | P20273 | Q3T9T5 | ||||||||||||
| Refseq | NM_001771 (mRNA) NP_001762 (protein) |
NM_001043317 (mRNA) NP_001036782 (protein) |
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| Location | Chr 19: 40.51 - 40.53 Mb | Chr 7: 30.57 - 30.59 Mb | ||||||||||||
| Pubmed search | [1] | [2] | ||||||||||||
CD22 or cluster of differentiation-22, is a molecule belonging to the SIGLEC family of lectins.[1] Generally speaking, CD22 is a regulatory molecule that prevents the overactivation of the immune system and the development of autoimmune diseases.
CD22 is a sugar binding transmembrane protein, which specifically binds sialic acid with an immunoglobulin (Ig) domain located at its N-terminus. The presence of Ig domains makes CD22 a member of the immunoglobulin superfamily. CD22 functions as an inhibitory receptor for B cell receptor (BCR) signalling.
An immunotoxin, BL22, that targets this receptor is being tested at the NIH.[2]
External links
Interactions
CD22 has been shown to interact with Grb2,[3][4] PTPN6,[5][4][6][7][8] LYN,[3][6] SHC1[3] and INPP5D.[3]
References
- ^ Crocker PR, Clark EA, Filbin M, Gordon S, Jones Y, Kehrl JH, Kelm S, Le Douarin N, Powell L, Roder J, Schnaar RL, Sgroi DC, Stamenkovic K, Schauer R, Schachner M, van den Berg TK, van der Merwe PA, Watt SM, Varki A (1998). "Siglecs: a family of sialic-acid binding lectins". Glycobiology 8 (2): v. doi:. PMID 9498912.
- ^ "BL22 Immunotoxin in Treating Patients Previously Treated With Cladribine for Hairy Cell Leukemia". ClinicalTrials.gov - U.S. National Institutes of Health. http://clinicaltrials.gov/ct/show/NCT00074048. Retrieved on 2008-02-19.
- ^ a b c d Poe, J C; Fujimoto M, Jansen P J, Miller A S, Tedder T F (Jun. 2000). "CD22 forms a quaternary complex with SHIP, Grb2, and Shc. A pathway for regulation of B lymphocyte antigen receptor-induced calcium flux". J. Biol. Chem. (UNITED STATES) 275 (23): 17420-7. doi:. ISSN 0021-9258. PMID 10748054.
- ^ a b Otipoby, K L; Draves K E, Clark E A (Nov. 2001). "CD22 regulates B cell receptor-mediated signals via two domains that independently recruit Grb2 and SHP-1". J. Biol. Chem. (United States) 276 (47): 44315-22. doi:. ISSN 0021-9258. PMID 11551923.
- ^ Blasioli, J; Paust S, Thomas M L (Jan. 1999). "Definition of the sites of interaction between the protein tyrosine phosphatase SHP-1 and CD22". J. Biol. Chem. (UNITED STATES) 274 (4): 2303-7. ISSN 0021-9258. PMID 9890995.
- ^ a b Greer, S F; Justement L B (May. 1999). "CD45 regulates tyrosine phosphorylation of CD22 and its association with the protein tyrosine phosphatase SHP-1". J. Immunol. (UNITED STATES) 162 (9): 5278-86. ISSN 0022-1767. PMID 10228003.
- ^ Law, C L; Sidorenko S P, Chandran K A, Zhao Z, Shen S H, Fischer E H, Clark E A (Feb. 1996). "CD22 associates with protein tyrosine phosphatase 1C, Syk, and phospholipase C-gamma(1) upon B cell activation". J. Exp. Med. (UNITED STATES) 183 (2): 547-60. ISSN 0022-1007. PMID 8627166.
- ^ Adachi, T; Wienands J, Wakabayashi C, Yakura H, Reth M, Tsubata T (Jul. 2001). "SHP-1 requires inhibitory co-receptors to down-modulate B cell antigen receptor-mediated phosphorylation of cellular substrates". J. Biol. Chem. (United States) 276 (28): 26648-55. doi:. ISSN 0021-9258. PMID 11356834.
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